A0A7J6M9F3 · A0A7J6M9F3_PEROL
- ProteinMultifunctional fusion protein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids3386 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic activity
- (6R)-NADHX = (6S)-NADHX
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 potassium ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 2367-2371 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: NNGGD | ||||||
Binding site | 2368 | K+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 2437 | K+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2441-2447 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: GTGLGRV | ||||||
Binding site | 2472 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2475 | K+ (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 2641 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 2707-2713 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: HLAELSR | ||||||
Binding site | 2747-2751 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KGATS | ||||||
Binding site | 2767-2776 | ATP (UniProtKB | ChEBI) | ||||
Sequence: NSGMGTAGSG | ||||||
Binding site | 2777 | (6S)-NADPHX (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | ADP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | ATP binding | |
Molecular Function | ATP-dependent NAD(P)H-hydrate dehydratase activity | |
Molecular Function | metal ion binding | |
Molecular Function | NADHX epimerase activity | |
Molecular Function | NADPHX epimerase activity | |
Biological Process | nicotinamide nucleotide metabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameATP-dependent (S)-NAD(P)H-hydrate dehydratase
- EC number
- Alternative names
- Recommended nameNAD(P)H-hydrate epimerase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Perkinsozoa > Perkinsea > Perkinsida > Perkinsidae > Perkinsus
Accessions
- Primary accessionA0A7J6M9F3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1605-1631 | Helical | ||||
Sequence: MLVLVISAILSPIATAIALLSCCHTML | ||||||
Transmembrane | 1652-1672 | Helical | ||||
Sequence: ITIALVAGLFYAIVHAAWLLI | ||||||
Transmembrane | 1678-1695 | Helical | ||||
Sequence: GLILVAVFAVGLVASIRM | ||||||
Transmembrane | 1716-1737 | Helical | ||||
Sequence: FWFQSLLMLALFTLINIVSSLF | ||||||
Transmembrane | 1769-1786 | Helical | ||||
Sequence: YLYSTIPGSLGGWLLAAL | ||||||
Transmembrane | 1798-1815 | Helical | ||||
Sequence: LIVSSIMTTTTGAMLWAI | ||||||
Transmembrane | 1900-1924 | Helical | ||||
Sequence: FMTWVFGQSLAWVAVCFVLLTGVAL | ||||||
Transmembrane | 2123-2143 | Helical | ||||
Sequence: VLFPVTGLVILLVLCLMESLL |
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 110-171 | |||||
Sequence: NEEHSRLKEGMESEIRKLKNTLATGDPETSTSTELSACLTHIAEASYAYNKLEDQLADLKTL | ||||||
Compositional bias | 228-248 | Basic and acidic residues | ||||
Sequence: TDEEHKNPWKRPVEECGRGGG | ||||||
Region | 228-252 | Disordered | ||||
Sequence: TDEEHKNPWKRPVEECGRGGGGSRD | ||||||
Compositional bias | 430-455 | Polar residues | ||||
Sequence: HAAKRESSAPSDNGQSQWTALRSPGD | ||||||
Region | 430-456 | Disordered | ||||
Sequence: HAAKRESSAPSDNGQSQWTALRSPGDS | ||||||
Region | 2230-2249 | Disordered | ||||
Sequence: LGLRHEGSGESTGTSVKRGV | ||||||
Domain | 2314-2530 | YjeF N-terminal | ||||
Sequence: MRRCDKNATDKYSIPSALLMENAGITSYRCLTELLPNSRMTPQTKVLVVCGPGNNGGDGFVVARYVHSNGGQVRVILLNSREKYHGDASTNLNIVDCIPGIPVEIATTEEAISAAVDWADVLVDGIFGTGLGRVVDPSSPFGMAIAAVNRAKKPVMSLDIPSGVNGDSGRIMGDQAVHATATATFGLVKVGNLVYPGREMCGNLTVTHIGYPPELYA | ||||||
Domain | 2534-2841 | YjeF C-terminal | ||||
Sequence: TYVNYFPPLPARSPAGHKGSFGKALFVAGAEGYYGAPMLSSYSFLKAGGGYSRLATVKSIIPVIAAEAPSIVFHELESTSAGSISSDNYDRVFKMAQHLADMVVVGPGVSTNGDTARLVRALVLSSEKPMVIDGDGLTAISAAPVDSTDIFSTASQLLQERHRKQLPPVVLTPHLAELSRLTGISMGELTDGSRSLLEVGRELAQKTNAVVVVKGATSMICEPSGRVRMNLSGNSGMGTAGSGDVLSGLIPAMYAAYGHEVDSLGDAVAAAVFLHGVAGDIAAINLRGEDGVTASDIMNAVPEAVSYV | ||||||
Compositional bias | 2882-2896 | Polar residues | ||||
Sequence: LSMSSSSSASSRPTE | ||||||
Region | 2882-2903 | Disordered | ||||
Sequence: LSMSSSSSASSRPTERPLQMPF | ||||||
Region | 3158-3231 | Disordered | ||||
Sequence: DQASQGRGVAKHRKKGKRGKRGRKGGSAKPSRSVPVPKIVAGPTTSPRVAASEVLRKPQEGAPEEENAEENIPV | ||||||
Compositional bias | 3166-3184 | Basic residues | ||||
Sequence: VAKHRKKGKRGKRGRKGGS | ||||||
Region | 3249-3301 | Disordered | ||||
Sequence: EMKENAESPRVECPSPSKETSSRCDHFCISTPNDSEATGPGMEHGLDEEEHDD | ||||||
Compositional bias | 3262-3285 | Polar residues | ||||
Sequence: PSPSKETSSRCDHFCISTPNDSEA |
Sequence similarities
Belongs to the NnrD/CARKD family.
Belongs to the NnrE/AIBP family.
In the C-terminal section; belongs to the NnrD/CARKD family.
In the N-terminal section; belongs to the NnrE/AIBP family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,386
- Mass (Da)370,119
- Last updated2021-04-07 v1
- ChecksumD6BE7B89B3305CAA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 228-248 | Basic and acidic residues | ||||
Sequence: TDEEHKNPWKRPVEECGRGGG | ||||||
Compositional bias | 430-455 | Polar residues | ||||
Sequence: HAAKRESSAPSDNGQSQWTALRSPGD | ||||||
Compositional bias | 2882-2896 | Polar residues | ||||
Sequence: LSMSSSSSASSRPTE | ||||||
Compositional bias | 3166-3184 | Basic residues | ||||
Sequence: VAKHRKKGKRGKRGRKGGS | ||||||
Compositional bias | 3262-3285 | Polar residues | ||||
Sequence: PSPSKETSSRCDHFCISTPNDSEA |